Open AccessThe Calponin Family Member CHDP-1 Interacts with Rac/CED-10 to Promote Cell Protrusions
Author(s) -
Lina Guan,
Xuehua Ma,
Jingyan Zhang,
Jiajia Li,
Yingchun Wang,
Mei Ding
Publication year - 2016
Publication title -
plos genetics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.587
H-Index - 233
eISSN - 1553-7404
pISSN - 1553-7390
DOI - 10.1371/journal.pgen.1006163
Subject(s) - cell cortex , microbiology and biotechnology , calponin , biology , cytoskeleton , actin , gtpase , actin cytoskeleton , rac1 , gtp binding protein regulators , motility , rac gtp binding proteins , g protein , cell , signal transduction , biochemistry
Eukaryotic cells extend a variety of surface protrusions to direct cell motility. Formation of protrusions is mediated by coordinated actions between the plasma membrane and the underlying actin cytoskeleton. Here, we found that the single calponin homology (CH) domain-containing protein CHDP-1 induces the formation of cell protrusions in C . elegans . CHDP-1 is anchored to the cortex through its amphipathic helix. CHDP-1 associates through its CH domain with the small GTPase Rac1/CED-10, which is a key regulator of the actin cytoskeleton. CHDP-1 preferentially binds to the GTP-bound active form of the CED-10 protein and preserves the membrane localization of GTP-CED-10. Hence, by coupling membrane expansion to Rac1-mediated actin dynamics, CHDP-1 promotes the formation of cellular protrusions in vivo .